Isolation, characterization, and location of a donor-acceptor unit from cross-linked fibrin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 66 ·No. 2 ·1970-06-00 ·Pages 472-9

Chen R, Doolittle RF

Abstract

The cross-linking systems of bovine and human fibrins were studied by the introduction of a radioactive substitute donor as an inhibitor of fibrin cross-linking, separation of the constituent polypeptide chains after sulfitolysis, and tryptic digestion of the labeled gamma-chains. The information gathered from this approach enabled us to isolate and characterize the complete donor-acceptor unit in tryptic digests of fibrin gamma-gamma cross-linked systems. In both bovine and human fibrin, this kind of cross-linking is accomplished by reciprocal bridging between overlapping carboxy-terminal segments of neighboring gamma-chains. The amino acid sequence of the carboxy-terminal heptadecapeptide of the bovine gamma-chain was determined and an alignment of the corresponding region of the human gamma-chain established.

MeSH Terms

Amino Acid Sequence Animals Carbon Isotopes Cattle Chromatography, Gel Electrophoresis Fibrin/isolation & purification Humans Methods Peptides/analysis

Chemicals

Carbon Isotopes Peptides Fibrin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Chen R

Doolittle R F

References (15)

15 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.66.2.472

Published

1970-06-00

Pages

472-9

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC283069

Subset

External Links

PubMed source DOI: 10.1073/pnas.66.2.472 PMC Full Text View journal details

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Isolation, characterization, and location of a donor-acceptor unit from cross-linked fibrin.

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